CD45 and Src-Related Protein Tyrosine Kinases Regulate the T Cell Response to Phorbol Esters
作者： Jan K. Czyzyk , Philip D. Fernsten , Teresa R. Brtva , Channing J. Der , John B. Winfield
关键词: Proto-oncogene tyrosine-protein kinase Src 、 Molecular biology 、 Transactivation 、 Chemistry 、 Receptor tyrosine kinase 、 c-Raf 、 PRKCQ 、 Jurkat cells 、 Protein kinase C 、 Protein tyrosine phosphatase 、 Biophysics 、 Cell biology 、 Biochemistry
摘要: Protein kinase C (PKC)-dependent activation of the Ras signal transduction cascade is essential for induction IL-2 promoter during stimulation T lymphocytes via cell receptor (TCR). In this study, effects PKC-activating phorbol myristate acetate (PMA) on Ras-dependent transcription from ets/AP-1 Ras-responsive element were examined in human cells. Pretreatment Jurkat cells with Src-family PTK inhibitor herbimycin A resulted a 50% inhibition transactivation reporter following incubation PMA. Evidence was also obtained to suggest participation leukocyte-specific protein tyrosine phosphatase CD45, regulator Src-like PTKs, PMA-induced Ras/Raf pathway. First, diminished 75% CD45-negative variants, compared CD45-positive Second, engagement CD45 by monoclonal antibodies suppresses PMA response construct. Taken together, these data that Src-related proteins mediate PKC-dependent pathway and implicate TCR-independent induced agents such as
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